Non-tight and tight chemomechanical couplings of biomolecular motors under hindering loads

Xie, Ping

doi:10.1016/j.jtbi.2020.110173

Cited by 12 publications

(12 citation statements)

References 112 publications

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“…We denote by k (+) the rate of ATP transition to ADP in the head with the forward NL orientation (e.g., the trailing head) and by k (−) the rate of ATP transition to ADP in the head without the forward NL orientation (e.g., the leading head). Rates k (+) and k (−) are independent of the force on the NLs, which are consistent with the available experimental data (see, e.g., [17][18][19] for detailed discussion). We denote by k D the rate of ADP release from the head bound to MT, which for simplicity is treated here to be independent of NL direction and force on NL.…”

Section: Dynamics Of Single Eg5-∆tail Moving On Single Mtsupporting

confidence: 89%

Effect of Kinesin-5 Tail Domain on Motor Dynamics for Antiparallel Microtubule Sliding

Liu

Wang

et al. 2021

IJMS

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Kinesin-5 motor consists of two pairs of heads and tail domains, which are situated at the opposite ends of a common stalk. The two pairs of heads can bind to two antiparallel microtubules (MTs) and move on the two MTs independently towards the plus ends, sliding apart the two MTs, which is responsible for chromosome segregation during mitosis. Prior experimental data showed that the tails of kinesin-5 Eg5 can modulate the dynamics of single motors and are critical for multiple motors to generate high steady forces to slide apart two antiparallel MTs. To understand the molecular mechanism of the tails modulating the ability of Eg5 motors, based on our proposed model the dynamics of the single Eg5 with the tails and that without the tails moving on single MTs is studied analytically and compared. Furthermore, the dynamics of antiparallel MT sliding by multiple Eg5 motors with the tails and that without the tails is studied numerically and compared. Both the analytical results for single motors and the numerical results for multiple motors are consistent with the available experimental data.

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Section: Dynamics Of Single Eg5-∆tail Moving On Single Mtsupporting

confidence: 89%

Effect of Kinesin-5 Tail Domain on Motor Dynamics for Antiparallel Microtubule Sliding

Liu

Wang

et al. 2021

IJMS

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“…where k is the ATPase rate of the motor, which is independent of F, as for the well-studied N-type kinesin-1. [39][40][41] As discussed in detail elsewhere, 31,[39][40][41] the argument of the load-independent ATPase rate for kinesin-1 is consistent with the available experimental data. [42][43][44][45] First, using Equations ( 8) and ( 9) we give an explanation of the experimental data of Molodtsov et al 21 As 8) and ( 9) it is noted only values of two parameters k and d 2 are required.…”

Section: Dynamics Of Kinesin-14 Cik1-kar3supporting

confidence: 83%

“…Consequently, after arriving at x = d 1 the motor takes a forward step and after arriving at x = − d 2 the motor takes a backward step. Then, the ratio of the probability of taking a forward step to that of taking a backward step (simply called stepping ratio) can be approximately calculated by

r = t_{2} / t_{1}

, which can be rewritten as

r = \frac{{d_{2}}^{2}}{{d_{1}}^{2}} \exp ((), - \frac{Fd}{k_{B} T}) .

With the stepping ratio r , the velocity of the motor can be written as

v = \frac{r - 1}{r + 1} italickd,

where k is the ATPase rate of the motor, which is independent of F , as for the well‐studied N‐type kinesin‐1 39–41 . As discussed in detail elsewhere, 31,39–41 the argument of the load‐independent ATPase rate for kinesin‐1 is consistent with the available experimental data 42–45 …”

Section: Resultsmentioning

confidence: 99%

Modeling processive motion of kinesin‐13 MCAK and kinesin‐14 Cik1‐Kar3 molecular motors

Xie

2021

Protein Science

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Kinesin-13 MCAK, which is composed of two identical motor domains, can undergo unbiased one-dimensional diffusion on microtubules. Kinesin-14 Cik1-Kar3, which is composed of a Kar3 motor domain and a Cik1 motor homology domain with no ATPase activity, can move processively toward the minus end of microtubules. Here, we present a model for the diffusion of MCAK homodimer and a model for the processive motion of Cik1-Kar3 heterodimer. Although the two dimeric motors show different domain composition, in the models it is proposed that the two motors use the similar physical mechanism to move processively. With the models, the dynamics of the two dimers is studied analytically. The theoretical results for MCAK reproduce quantitatively the available experimental data about diffusion constant and lifetime of the motor bound to microtubule in different nucleotide states. The theoretical results for Cik1-Kar3 reproduce quantitatively the available experimental data about load dependence of velocity and explain consistently the available experimental data about effects of the exchange and mutation of the motor homology domain on the velocity of the heterodimer. Moreover, predicted results for other aspects of the dynamics of the two dimers are provided.

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“…Motor proteins or biomolecular motors are a group of macromolecules that typically consume the energy of a chemical reaction and convert it into mechanical motion or work to perform a myriad of biological functions in cells [1,2]. A large number of molecular motors can move processively on their linear tracks [3]. A typical class in this category is that of kinesin proteins, which can move processively on microtubule (MT) filaments towards the plus end by hydrolyzing ATP molecules, responsible for intracellular transport, chromosome segregation during mitosis, regulation of MT dynamics and so on [4][5][6][7].…”

Section: Introductionmentioning

confidence: 99%

Insight into the chemomechanical coupling mechanism of kinesin molecular motors

Xie¹

2021

Commun. Theor. Phys.

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Kinesin is a two-headed biological molecular motor that can walk processively on microtubule via consumption of ATP molecules. The central issue for the molecular motor is how the chemical energy released from ATP hydrolysis is converted to the kinetic energy of the mechanical motion, namely the mechanism of chemomechanical coupling. To address the issue, diverse experimental methods have been employed and a lot of models have been proposed. This review focuses on the proposed models as well as the qualitative and quantitative comparisons between the results derived from the models and those from the structural, biochemical and single-molecule experimental studies.

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Non-tight and tight chemomechanical couplings of biomolecular motors under hindering loads

Cited by 12 publications

References 112 publications

Effect of Kinesin-5 Tail Domain on Motor Dynamics for Antiparallel Microtubule Sliding

Effect of Kinesin-5 Tail Domain on Motor Dynamics for Antiparallel Microtubule Sliding

Modeling processive motion of kinesin‐13 MCAK and kinesin‐14 Cik1‐Kar3 molecular motors

Insight into the chemomechanical coupling mechanism of kinesin molecular motors

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